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Interactions between CLIP-170, Tubulin, and Microtubules: Implications for the Mechanism of CLIP-170 Plus-End Tracking Behavior | Molecular Biology of the Cell
Selective visualization of growing MT ends with CLIP170. CHO cells were... | Download Scientific Diagram
![Tension of plus-end tracking protein Clip170 confers directionality and aggressiveness during breast cancer migration | Cell Death & Disease Tension of plus-end tracking protein Clip170 confers directionality and aggressiveness during breast cancer migration | Cell Death & Disease](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs41419-022-05306-6/MediaObjects/41419_2022_5306_Fig1_HTML.png)
Tension of plus-end tracking protein Clip170 confers directionality and aggressiveness during breast cancer migration | Cell Death & Disease
Subcellular distribution of CLIP-170 throughout the mitotic cycle of... | Download Scientific Diagram
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Quelle fonction pour la CLIP-170? : recherche de partenaires et nouveaux outils d'investigation | Semantic Scholar
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CLIP‐170 spatially modulates receptor tyrosine kinase recycling to coordinate cell migration - Zaoui - 2019 - Traffic - Wiley Online Library
Overexpression of the microtubule-binding protein CLIP-170 induces a +TIP network superstructure consistent with a biomolecular
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Conformational changes in CLIP-170 regulate its binding to microtubules and dynactin localization. - Abstract - Europe PMC
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Phosphorylation of CLIP‐170 by Plk1 and CK2 promotes timely formation of kinetochore–microtubule attachments | The EMBO Journal
![Phosphorylation of CLIP‐170 by Plk1 and CK2 promotes timely formation of kinetochore–microtubule attachments | The EMBO Journal Phosphorylation of CLIP‐170 by Plk1 and CK2 promotes timely formation of kinetochore–microtubule attachments | The EMBO Journal](https://www.embopress.org/cms/asset/aa4ee24b-6584-430e-b994-5948f482cc5b/embj2010174-fig-0007-m.jpg)
Phosphorylation of CLIP‐170 by Plk1 and CK2 promotes timely formation of kinetochore–microtubule attachments | The EMBO Journal
![Ninein is essential for apico-basal microtubule formation and CLIP-170 facilitates its redeployment to non-centrosomal microtubule organizing centres | Open Biology Ninein is essential for apico-basal microtubule formation and CLIP-170 facilitates its redeployment to non-centrosomal microtubule organizing centres | Open Biology](https://royalsocietypublishing.org/cms/asset/34ee49bb-1c76-4868-a860-f9762bde3a23/rsob160274f08.jpg)
Ninein is essential for apico-basal microtubule formation and CLIP-170 facilitates its redeployment to non-centrosomal microtubule organizing centres | Open Biology
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Ninein is essential for apico-basal microtubule formation and CLIP-170 facilitates its redeployment to non-centrosomal microtubule organizing centres | Open Biology
![CLIP-170 is essential for MTOC repositioning during T cell activation by regulating dynein localisation on the cell surface | Scientific Reports CLIP-170 is essential for MTOC repositioning during T cell activation by regulating dynein localisation on the cell surface | Scientific Reports](https://media.springernature.com/lw685/springer-static/image/art%3A10.1038%2Fs41598-018-35593-z/MediaObjects/41598_2018_35593_Fig2_HTML.png)
CLIP-170 is essential for MTOC repositioning during T cell activation by regulating dynein localisation on the cell surface | Scientific Reports
Overexpression of the microtubule-binding protein CLIP-170 induces a +TIP network superstructure consistent with a biomolecular condensate | PLOS ONE
![α-Tubulin Tyrosination and CLIP-170 Phosphorylation Regulate the Initiation of Dynein-Driven Transport in Neurons - ScienceDirect α-Tubulin Tyrosination and CLIP-170 Phosphorylation Regulate the Initiation of Dynein-Driven Transport in Neurons - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S221112471630167X-fx1.jpg)
α-Tubulin Tyrosination and CLIP-170 Phosphorylation Regulate the Initiation of Dynein-Driven Transport in Neurons - ScienceDirect
![Microtubule binding proteins CLIP-170, EB1, and p150Glued form distinct plus-end complexes - ScienceDirect Microtubule binding proteins CLIP-170, EB1, and p150Glued form distinct plus-end complexes - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0014579306001037-gr4.jpg)